Cell-free eukaryotic systems for the production, engineering, and modification of scFv antibody fragments

Engineering in Life Sciences

Volumn 14, Issue 4, 2014, Pages 387-398

  Stech, Marlitt ^a   Hust, Michael ^b   Schulze, Corina ^c   Dübel, Stefan ^b   Kubick, Stefan ^a  

^a FRAUNHOFER INSTITUTE FOR CELL THERAPY AND IMMUNOLOGY   (Germany)

^b TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^c UNIVERSITY OF APPLIED SCIENCES   (Germany)

Author keywords

Cell free; ELISA; Insect cell extract; ScFv antibody fragment; Sf21 insect lysate

Indexed keywords

AMINO ACIDS; CELLS; CYTOLOGY; EPITOPES; ESCHERICHIA COLI; MOLECULES; PEPTIDES; SYNTHESIS (CHEMICAL);

CELL-FREE; ELISA; INSECT CELLS; SCFV ANTIBODY FRAGMENTS; SF21 INSECT LYSATE;

ANTIBODIES;

AMINO ACID; CELL EXTRACT; CHEMOKINE RECEPTOR CXCR5; MELITTIN; SIGNAL PEPTIDE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; SMAD2 PROTEIN;

AMINO ACID; ANIMAL PRODUCT; ANTIBODY; ANTIGEN; BIOLOGICAL PRODUCTION; COLIFORM BACTERIUM; EUKARYOTE; INDUSTRIAL PRODUCTION; INSECT; TOXIN;

ANTIGEN BINDING; ARTICLE; CELL LYSATE; CENTRIFUGATION; CYTOSOL; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; INSECT; NONHUMAN; POLYMERASE CHAIN REACTION; PROTEIN SYNTHESIS; RNA TRANSLATION;

EID: 84904347110     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201400036     Document Type: Article

References (54)

1. Weisser, N. E., Hall, J. C., Applications of single-chain variable fragment antibodies in therapeutics and diagnostics. Biotechnol. Adv. 2009, 27, 502-520.
2. Colwill, K., Graslund, S., A roadmap to generate renewable protein binders to the human proteome. Nat. Meth. 2011, 8, 551-558.
3. Hagemeyer, C., von Zur Muhlen, C., von Elverfeldt, D., Peter, K., Single-chain antibodies as diagnostic tools and therapeutic agents. Thromb. Haemost. 2009 101, 1012-1019.
4. Bundy, B. C., Swartz, J. R., Efficient disulfide bond formation in virus-like particles. J. Biotechnol. 2011, 154, 230-239.
5. Kim, D.-M., Swartz, J. R., Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol. Bioeng. 2004, 85, 122-129.
6. Merk, H., Stiege, W., Tsumoto, K., Kumagai, I. et al., Cell-free expression of two single-chain monoclonal antibodies against lysozyme: Effect of domain arrangement on the expression. J. Biochem. (Tokyo) 1999, 125, 328-333.
7. Oh, I.-S., Lee, J.-C., Lee, M.-S., Chung, J.-H. et al., Cell-free production of functional antibody fragments. Bioproc. Biosyst. Eng. 2010, 33, 127-132.
8. Ryabova, L. A., Desplancq, D., Spirin, A. S., Plückthun, A., Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. Nat. Biotechnol. 1997, 15, 79-84.
9. Carlson, E. D., Gan, R., Hodgman, C. E., Jewett, M. C., Cell-free protein synthesis: Applications come of age. Biotechnol. Adv. 2012, 30, 1185-1194.
10. Rungpragayphan, S., Nakano, H., Yamane, T., PCR-linked in vitro expression: A novel system for high-throughput construction and screening of protein libraries. FEBS Lett. 2003, 540, 147-150.
11. Yin, G., Garces, E. D., Yang, J., Zhang, J., et al., Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system. mAbs 2012, 4, 217-225.
12. Kanter, G., Yang, J., Voloshin, A., Levy, S. et al., Cell-free production of scFv fusion proteins: An efficient approach for personalized lymphoma vaccines. Blood 2007, 109, 3393-3399.
13. Patel, K. G., Ng, P. P., Levy, S., Levy, R. et al., Escherichia coli-based production of a tumor idiotype antibody fragment-Tetanus toxin fragment C fusion protein vaccine for B cell lymphoma. Protein Expres. Purif. 2011, 75, 15-20.
14. Jiang, X., Ookubo, Y., Fujii, I., Nakano, H. et al., Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system. FEBS Lett. 2002, 514, 290-294.
15. Kawasaki, T., Gouda, M. D., Sawasaki, T., Takai, K. et al., Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ. Eur. J. Biochem. 2003, 270, 4780-4786.
16. Merk, H., Gless, C., Maertens, B., Gerrits, M. et al., Cell-free synthesis of functional and endotoxin-free antibody Fab fragments by translocation into microsomes. BioTechniques 2012, 53, 153-160.
17. Stech, M., Merk, H., Schenk, J., Stöcklein, W. et al., Production of functional antibody fragments in a vesicle-based eukaryotic cell-free translation system. J. Biotechnol. 2012, 164, 220-231.
18. Alzari, P., Lascombe, M., Poljak, R., Three-dimensional structure of antibodies. Annu. Rev. Immunol. 1988, 6, 555-580.
19. Davies, D., Padlan, E., Sheriff, S., Antibody-antigen complexes. Annu. Rev. Biochem. 1990, 59, 439-473.
20. Glockshuber, R., Schmidt, T., Plückthun, A., The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in Escherichia coli. Biochemistry 1992, 31, 1270-1279.
21. Goto, Y., Hamaguchi, K., The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 1979, 86, 1433-1441.
22. Brödel, A. K., Raymond, J. A., Duman, J. G., Bier, F. F. et al., Functional evaluation of candidate ice structuring proteins using cell-free expression systems. J. Biotechnol. 2013, 163, 301-310.
23. Bird, R., Hardman, K., Jacobsen, J., Johnson, S. et al., Single-chain antigen-binding proteins. Science 1988, 242, 423-426.
24. Huston, J., Levinson, D., Mudgett, H., Tai, M. et al., Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digosin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 1988, 85, 5879-5883.
25. Kubick, S., Gerrits, M., Merk, H., Stiege, W. et al., In vitro synthesis of posttranslationally modified membrane proteins, in: DeLucas, L. (Ed.), "Membrane Protein Crystallization" Current Topics in Membranes, Chapter 2, Elsevier, Burlington 2009, pp. 25-49.
26. Kubick, S., Schacherl, J., Fleischer-Notter, H., Royall, E. et al., In vitro translation in an insect-based cell-free system, in: Swartz, J. R. (Ed.), Cell-Free Protein Expression, Springer, Berlin, Heidelberg/New York 2003, pp. 209-217.
27. Sachse, R., Wüstenhagen, D., Šamalíková, M., Gerrits, M. et al., Synthesis of membrane proteins in eukaryotic cell-free systems. Eng. Life Sci. 2013, 13, 39-48.
28. Stech, M., Brödel, A. K., Quast, R. B., Sachse, R. et al., Advances in Biochemical Engineering/Biotechnology, Springer, Berlin Heidelberg 2013, pp. 67-102.
29. Brödel, A., Sonnabend, A., Roberts, L., Stech, M. et al., IRES-mediated translation of membrane proteins and glycoproteins in eukaryotic cell-free systems. PLoS One 2013, 8, e82234.
30. Hust, M., Meyer, T., Voedisch, B., Rülker, T. et al., A human scFv antibody generation pipeline for proteome research. J. Biotechnol. 2011, 152, 159-170.
31. Schirrmann, T., Hust, M., Construction of human antibody gene libraries and selection of antibodies by phage display. Methods Mol. Biol. 2010, 651, 177-209.
32. Merk, H., Meschkat, D., Stiege, W., Expression-PCR: From gene pools to purified proteins within 1 day, in: Swartz, J. R. (Ed.), Cell-Free Protein Expression, Springer, Berlin Heidelberg/New York 2003, pp. 15-23.
33. Tessier, D. C., Thomas, D. Y., Khouri, H. E., Laliberié, F. et al., Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide. Gene 1991, 98, 177-183.
34. Hust, M., Steinwand, M., Al-Halabi, L., Helmsing, S. et al., Improved microtitre plate production of single chain Fv fragments in Escherichia coli. New Biotechnol. 2009, 25, 424-428.
35. Mollova, S., Retter, I., Hust, M., Dübel, S. et al., Analysis of single chain antibody sequences using the VBASE2 Fab analysis tool, in: Kontermann, R. (Ed.), Antibody Engineering, Springer, Berlin Heidelberg 2010, pp. 3-10.
36. Kaufman, R. J., Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev. 1999, 13, 1211-1233.
37. Micheel, B., Jantscheff, P., Böttger, V., Scharte, G. et al., The production and radioimmunoassay application of monoclonal antibodies to fluorescein isothiocyanate (FITC). J. Immunol. Methods 1988, 111, 89-94.
38. Schenk, J. A., Sellrie, F., Böttger, V., Menning, A. et al., Generation and application of a fluorescein-specific single chain antibody. Biochimie 2007, 89, 1304-1311.
39. Tu, T., Weissman, J., Oxidative protein folding in eukaryotes mechanisms and consequences. J. Cell Biol. 2004, 164, 341-346.
40. Kierzek, A. M., Zaim, J., Zielenkiewicz, P., The effect of transcription and translation initiation frequencies on the stochastic fluctuations in prokaryotic gene expression. J. Biol. Chem. 2001, 276, 8165-8172.
41. Sonenberg, N., Hinnebusch, A., Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 2009, 136, 731-745.
42. Ahn, J.-H., Hwang, M.-Y., Lee, K.-H., Choi, C.-Y. et al., Use of signal sequences as an in situ removable sequence element to stimulate protein synthesis in cell-free extracts. Nucleic Acids Res. 2007, 35, e21.
43. Kigawa, T., Yabuki, T., Yoshida, Y., Tsutsui, M. et al., Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 1999, 442, 15-19.
44. Tarui, H., Murata, M., Tani, I., Imanishi, S. et al., Establishment and characterization of translation/glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment. Appl. Microbiol. Biotechnol. 2001, 55, 446-453.
45. Vinarov, D. A., Lytle, B. L., Peterson, F. C., Tyler, E. M. et al., Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Meth. 2004, 1, 149-153.
46. Stech, M., Quast, R. B., Sachse, R., Schulze, C., Wüstenhagen, D.A., Kubick, S., A continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells. PLoS One 2014, e96635.
47. Shimizu, Y., Kuruma, Y., Ying, B.-W., Umekage, S. et al., Cell-free translation systems for protein engineering. FEBS J. 2006, 273, 4133-4140.
48. Axup, J. Y., Bajjuri, K. M., Ritland, M., Hutchins, B. M. et al., Synthesis of site-specific antibody-drug conjugates using unnatural amino acids. Proc. Natl. Acad. Sci. 2012, 109, 16101-16106.
49. Zimmerman, E. S., Heibeck, T. H., Gill, A., Li, X. et al., Production of site-specific antibody-drug conjugates using optimized non-natural amino acids in a cell-free expression system. Bioconjugate Chem. 2014, 25, 351-361.
50. Quast, R. B., Claussnitzer, I., Merk, H., Kubick, S. et al., Synthesis and site-directed fluorescence labeling of azido proteins using eukaryotic cell-free orthogonal translation systems. Anal. Biochem. 2014, 451, 4-9.
51. Kumar Dondapati, S., Kreir, M., Quast, R. B., Wüstenhagen, D. A. et al., Membrane assembly of the functional KcsA potassium channel in a vesicle-based eukaryotic cell-free translation system. Biosens. Bioelectron. 2014, 59, 174-183.
52. Fenz, S. F., Sachse, R., Schmidt, T., Kubick, S., Cell-free synthesis of membrane proteins: Tailored cell models out of microsomes. Biochim. Biophys. Acta 2014, 1838, 1382-1388.
53. Shaklee, P. M., Semrau, S., Malkus, M., Kubick, S. et al., Protein incorporation in giant lipid vesicles under physiological conditions. ChemBioChem 2010, 11, 175-179.
54. Zawada, J. F., Yin, G., Steiner, A. R., Yang, J. et al., Microscale to manufacturing scale-up of cell-free cytokine production-A new approach for shortening protein production development timelines. Biotechnol. Bioeng. 2011, 108, 1570-1578.